Specific disease related glycosylation changes for glycans released from purified serum IgG were first reported for rheumatoid arthritis, see Parekh et. al. “Association of Rheumatoid Arthritis and Primary Osteoarthritis with Changes in the Glycosylation Pattern of Total Serum IgG,” Nature, 316, pp. 452-457, 1985, incorporated herein by reference. Subsequent work demonstrated that these changes were not only diagnostic of rheumatoid arthritis (RA), but could also be used as prognostic indicators as well as monitors of RA disease activity, see e.g. “Galactosylation of IgG associated oligosaccharides: Reduction in patients with adult and juvenile onset rheumatoid arthritis and relation to disease activity,” R. B. Parekh, D. A. Isenberg, B. M. Ansell, I. M. Roitt, R. A. Dwek and T. W. Rademacher (1988) Lancet, 1(8592), 966-969; “A comparative analysis of disease-associated changes in the galactosylation of serum IgG” R. B. Parekh, D. Isenberg, G. Rook, I. Roitt, R. A. Dwek and T. W. Rademacher (1989) J. Autoimmunity, 2, 101-114; 3rd Jenner International Immunoglycobiology Meeting Abstract R. B. Parekh, Isenberg, D., Dwek, R. A. and Rademacher, T. W. Glycoconjugate Journal (1994) 1, 3 195-227, all incorporated herein by reference in their entirety. Later, it was demonstrated that specific glycosylation changes in total serum glycosylation can be also bio-markers of other diseases. For example, Block et. al. determined specific glycosylation changes in total serum of hepatocellular carcinoma woodchucks infected with hepatitis B virus by performing a glycosylation analysis on glycans enzymatically released from a total serum solution, i.e. by a method not compatible with a high throughput format, see Block, T. M., Comunale, M. A., Lowman, M., Steel, L. F., Romano, P. R., Fimmel, C., Tennant, B. C., London, W. T., Evans, A. A., Blumberg, B. S., Dwek, R. A., Mattu, T. S. and Mehta, A. S. (2005). “Use of targeted glycoproteomics to identify serum glycoproteins that correlate with liver cancer in woodchucks and humans.” Proc Natl Acad Sci USA 102: 779-84, incorporated herein by reference in its entirety. Glycosylation analysis of whole serum glycoproteins from patients and healthy controls using a combination of high-performance liquid chromatography (HPLC) (see Guile, G. R., et. al., “A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles.” Anal. Biochem. 240: 210-26, 1996; Royle, L., et. al. “An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins.” Anal. Biochem. 304: 70-90, 2002) and Mass Spectrometry (MS) technology was first used to confirm the diagnosis of a patient with congenital disorders of glycosylation (CDGs) type II and to establish the faulty glycosylation processing step in an undiagnosed patient, see Butler, M., et. al. “Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis.” Glycobiology 13: 601-22, 2003. The glycan profile and analysis were flawed because hydrazinolysis was used to release the glycans. The use of hydrazinolysis results in the desialylation of a significant proportion of the sugars and the introduction of a number of artifacts such as loss of N-acetyl and N-glycolyl groups from the amino sugar residues (which are subsequently re-N-acetylated and this can result in both under and over acetylation), as well as loss of O-acetyl substitutions in sialic acids. Callewaert et al. used enzymatic release in whole serum glycosylation analysis by capillary electrophoresis on a microfluidic platform, see Callewaert, N., Contreras, R., Mitnik-Gankin, L., Carey, L., Matsudaira, P. and Ehrlich, D. (2004). “Total serum protein N-glycome profiling on a capillary electrophoresis-microfluidics platform.” Electrophoresis 25: 3128-31 and Callewaert, N., Schollen, E., Vanhecke, A., Jaeken, J., Matthijs, G., and Contreras, R. (2003). “Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I.” Glycobiology 13: 367-375. Although enzymatic release of Callewaert et. al. is compatible with a high throughput format, their analyses determined only major desialylated structures. Thus, a need still exists to develop a high throughput fully automated method for determining robust glycosylation markers of diseases based on a detailed glycosylation analysis of total glycoproteins in samples of body fluid or body tissue.